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Database: UniProt
Entry: G7YGQ7_CLOSI
LinkDB: G7YGQ7_CLOSI
Original site: G7YGQ7_CLOSI 
ID   G7YGQ7_CLOSI            Unreviewed;       947 AA.
AC   G7YGQ7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Alpha-aminoadipic semialdehyde synthase {ECO:0000313|EMBL:GAA52140.1, ECO:0000313|EMBL:KAG5451549.1};
GN   ORFNames=CLF_107394 {ECO:0000313|EMBL:GAA52140.1}, CSKR_104315
GN   {ECO:0000313|EMBL:KAG5451549.1};
OS   Clonorchis sinensis (Chinese liver fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX   NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA52140.1, ECO:0000313|Proteomes:UP000008909};
RN   [1] {ECO:0000313|EMBL:GAA52140.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Henan {ECO:0000313|EMBL:GAA52140.1};
RX   PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA   Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA   Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA   Yu X.;
RT   "The draft genome of the carcinogenic human liver fluke Clonorchis
RT   sinensis.";
RL   Genome Biol. 12:R107-R107(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Henan;
RA   Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA   Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA   Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA   Wu Z., Yu X.;
RT   "The genome and transcriptome sequence of Clonorchis sinensis provide
RT   insights into the carcinogenic liver fluke.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAG5451549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5451549.1};
RX   PubMed=29454982;
RA   Wang D., Korhonen P.K., Gasser R.B., Young N.D.;
RT   "Improved genomic resources and new bioinformatic workflow for the
RT   carcinogenic parasite Clonorchis sinensis: Biotechnological implications.";
RL   Biotechnol. Adv. 36:894-904(2018).
RN   [4] {ECO:0000313|EMBL:KAG5451549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5451549.1};
RX   PubMed=33677057;
RA   Young N.D., Stroehlein A.J., Kinkar L., Wang T., Sohn W.M., Chang B.C.H.,
RA   Kaur P., Weisz D., Dudchenko O., Aiden E.L., Korhonen P.K., Gasser R.B.;
RT   "High-quality reference genome for Clonorchis sinensis.";
RL   Genomics 0:0-0(2021).
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 1/6.
CC       {ECO:0000256|ARBA:ARBA00004682}.
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 2/6.
CC       {ECO:0000256|ARBA:ARBA00004720}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005624}.
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DR   EMBL; DF143246; GAA52140.1; -; Genomic_DNA.
DR   EMBL; NIRI02000042; KAG5451549.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7YGQ7; -.
DR   STRING; 79923.G7YGQ7; -.
DR   InParanoid; G7YGQ7; -.
DR   UniPathway; UPA00868; UER00835.
DR   Proteomes; UP000008909; Unassembled WGS sequence.
DR   Proteomes; UP000286415; Chromosome 1.
DR   GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   CDD; cd12189; LKR_SDH_like; 1.
DR   Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008909}.
FT   DOMAIN          38..172
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          212..416
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   947 AA;  105010 MW;  B574C63A2BB0B6F5 CRC64;
     MFARLSVPRL CMSGVCSTLH GTPRRSVNRA SLSRPVVGIK RETVNLWEQR SPLTPSQVHQ
     LISQHGVRVL VQPSNRRCFT SSEYEAAGAE IAENLEDATL ILGVKRPAEL RPHDLLQDKT
     YAFFTHTIKA QPANMTLLDT LFERNIRIID YECMVNEHNK RVVAFGQHAG MAGTIDIIHG
     LGIRLLALGH RTPFMHVSIA HNYHNLNEAQ QAIRLVGYEL ALGRLPASIG PLVFVINGDG
     NVAQGAEKIL NNLPAKSISP RELQHVANQG ETNVIYLCKV NPSHYMEHKD GKPFVEEEYF
     RKPEDYKSNF INKIAPYTSV LINATYWDSR IDRILTRENV KSLIDVKPNV SGSPLNEACP
     TLPYRMIAIC DISADSNGSI EFTDECTTID EPFVLYDPRT DKEKRTIAGD GILMCSIDNL
     PAQLPFEASE HFGTALIPYL PDMVKSDATQ PFDRYNAGPV VKNAIIASNG ALTPKFQYID
     SLRKKTGLSS TSTSSKKVLI LGAGYVVPPV IEYLSRDKSV ELTVVSNIYD ELSELARHYP
     NILARNVNVL EDNQSLANLI QNSDLVLSLI PWRFHPTVVT ECVKQKRNLL TASYCTPNLK
     EMESSIQQAG ITAVMEIGLD PGIDHLLTKE CIDDVRAKGG RVISYRSYTG GLPAPENSSN
     PLRYKFSWSP EAALSTVMNG AKYLENGKIK EVPADGSLMK MASPMNLFPG FNLEGYPNRD
     STRYIDLYGL TGCETVIRGT LRYSGYANAV LFMLDLGLLQ THQEAHLRPG AQKLSWRELI
     CQKLGLHNQL TGNELRRAVL SKLEGNQAKY DCLNELGFLS DDTVAQAGTP LASTALQLSR
     YLSYGPNERD LIIMAHELTI DWPDKKQREY RKVSLVAYGT AGQGKAGLAM SRTVGLPAAI
     AAKMILDGEI TEKGIVLPLK PEIYKPILEK LKTEGIEAHE TSTFCDM
//
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